SitesBLAST
Comparing WP_011022811.1 NCBI__GCF_000007345.1:WP_011022811.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
7vo1A Structure of aminotransferase-substrate complex (see paper)
45% identity, 89% coverage: 51:473/477 of query aligns to 7:441/452 of 7vo1A
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid: I61 (= I103), S121 (= S160), G122 (= G161), T123 (= T162), F149 (= F188), H150 (= H189), R152 (= R191), E234 (= E267), D262 (= D295), V264 (= V297), Q265 (= Q298), K291 (= K324), N318 (= N351), T319 (= T352), R417 (= R449)
7vntA Structure of aminotransferase-substrate complex (see paper)
45% identity, 89% coverage: 51:473/477 of query aligns to 7:441/452 of 7vntA
- binding L-ornithine: F149 (= F188), R152 (= R191), E234 (= E267), K291 (= K324)
- binding pyridoxal-5'-phosphate: G122 (= G161), T123 (= T162), F149 (= F188), H150 (= H189), E229 (= E262), D262 (= D295), V264 (= V297), Q265 (= Q298), K291 (= K324)
7vnoA Structure of aminotransferase (see paper)
45% identity, 89% coverage: 51:473/477 of query aligns to 7:441/452 of 7vnoA
O50131 Ornithine aminotransferase; Orn-AT; Ornithine delta-aminotransferase; EC 2.6.1.13 from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) (see paper)
45% identity, 89% coverage: 51:473/477 of query aligns to 9:443/454 of O50131
- T92 (≠ G132) mutation to V: Slightly increases the specific activity. Increases KM for L-ornithine.
- D93 (= D133) mutation to L: Reduces the specific activity. Increases KM for L-ornithine.
- G124 (= G161) binding pyridoxal 5'-phosphate
- T125 (= T162) binding pyridoxal 5'-phosphate
- Q267 (= Q298) binding pyridoxal 5'-phosphate
- K293 (= K324) modified: N6-(pyridoxal phosphate)lysine
- T321 (= T352) binding pyridoxal 5'-phosphate
O58478 Alanine/serine racemase; ASR; Ala/Ser racemase; EC 5.1.1.-; EC 5.1.1.1 from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) (see paper)
37% identity, 88% coverage: 54:473/477 of query aligns to 29:459/474 of O58478
- D251 (≠ E267) mutation to A: Loss of activity.
- K308 (= K324) mutation to A: Loss of activity.
2eo5A Crystal structure of 4-aminobutyrate aminotransferase from sulfolobus tokodaii strain7
40% identity, 87% coverage: 57:473/477 of query aligns to 3:410/412 of 2eo5A
- active site: T18 (≠ V72), F139 (= F188), E219 (= E262), D252 (= D295), Q255 (= Q298), K281 (= K324), T303 (= T352), R386 (= R449)
- binding pyridoxal-5'-phosphate: G113 (= G161), T114 (= T162), F139 (= F188), H140 (= H189), E219 (= E262), D252 (= D295), V254 (= V297), Q255 (= Q298), K281 (= K324)
P22256 4-aminobutyrate aminotransferase GabT; 5-aminovalerate transaminase; GABA aminotransferase; GABA-AT; Gamma-amino-N-butyrate transaminase; GABA transaminase; Glutamate:succinic semialdehyde transaminase; L-AIBAT; EC 2.6.1.19; EC 2.6.1.48 from Escherichia coli (strain K12) (see 2 papers)
35% identity, 88% coverage: 58:477/477 of query aligns to 5:426/426 of P22256
- I50 (= I103) mutation to Q: 3-fold decrease in catalytic activity and 12-fold decrease in affinity for GABA.
- GS 111:112 (≠ GT 161:162) binding pyridoxal 5'-phosphate
- E211 (= E267) mutation to S: 100-fold decrease in catalytic activity and 15-fold decrease in affinity for GABA.
- V241 (= V297) mutation to A: 25-fold decrease in catalytic activity and 5-fold decrease in affinity for GABA.
- Q242 (= Q298) binding pyridoxal 5'-phosphate
- K268 (= K324) modified: N6-(pyridoxal phosphate)lysine
- T297 (= T352) binding pyridoxal 5'-phosphate
1sffA Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (see paper)
35% identity, 88% coverage: 58:477/477 of query aligns to 4:425/425 of 1sffA
- active site: V18 (= V72), Y137 (≠ F188), E205 (= E262), D238 (= D295), Q241 (= Q298), K267 (= K324), T296 (= T352), R397 (= R449)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Q78 (≠ G132), G110 (= G161), S111 (≠ T162), Y137 (≠ F188), H138 (= H189), R140 (= R191), E205 (= E262), D238 (= D295), V240 (= V297), Q241 (= Q298), K267 (= K324), T296 (= T352)
- binding sulfate ion: N152 (≠ R204), Y393 (vs. gap)
1sf2A Structure of e. Coli gamma-aminobutyrate aminotransferase (see paper)
35% identity, 88% coverage: 58:477/477 of query aligns to 4:425/425 of 1sf2A
- active site: V18 (= V72), Y137 (≠ F188), E205 (= E262), D238 (= D295), Q241 (= Q298), K267 (= K324), T296 (= T352), R397 (= R449)
- binding pyridoxal-5'-phosphate: G110 (= G161), S111 (≠ T162), Y137 (≠ F188), H138 (= H189), E205 (= E262), D238 (= D295), V240 (= V297), Q241 (= Q298), K267 (= K324)
- binding sulfate ion: N152 (≠ R204), Y393 (vs. gap)
1szkA The structure of gamma-aminobutyrate aminotransferase mutant: e211s (see paper)
35% identity, 88% coverage: 58:477/477 of query aligns to 4:425/425 of 1szkA
- active site: V18 (= V72), Y137 (≠ F188), E205 (= E262), D238 (= D295), Q241 (= Q298), K267 (= K324), T296 (= T352), R397 (= R449)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G110 (= G161), S111 (≠ T162), Y137 (≠ F188), H138 (= H189), E205 (= E262), D238 (= D295), V240 (= V297), Q241 (= Q298), K267 (= K324)
P50457 4-aminobutyrate aminotransferase PuuE; GABA aminotransferase; GABA-AT; Gamma-amino-N-butyrate transaminase; GABA transaminase; Glutamate:succinic semialdehyde transaminase; EC 2.6.1.19 from Escherichia coli (strain K12) (see paper)
36% identity, 82% coverage: 83:472/477 of query aligns to 29:419/421 of P50457
- K267 (= K324) mutation to A: No GABA-AT activity.
4addA Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
37% identity, 84% coverage: 72:471/477 of query aligns to 15:394/400 of 4addA
- active site: F136 (= F188), E188 (= E262), D221 (= D295), Q224 (= Q298), K250 (= K324), T279 (= T352), R372 (= R449)
- binding pyridoxal-5'-phosphate: G103 (= G161), A104 (≠ T162), F136 (= F188), H137 (= H189), D221 (= D295), V223 (= V297), K250 (= K324)
- binding n~2~-(3-carboxypropanoyl)-l-ornithine: Y16 (≠ S73), F136 (= F188), R139 (= R191)
4adbB Structural and functional study of succinyl-ornithine transaminase from e. Coli (see paper)
37% identity, 84% coverage: 72:471/477 of query aligns to 15:394/401 of 4adbB
- active site: F136 (= F188), E188 (= E262), D221 (= D295), Q224 (= Q298), K250 (= K324), T279 (= T352), R372 (= R449)
- binding pyridoxal-5'-phosphate: S102 (= S160), G103 (= G161), A104 (≠ T162), F136 (= F188), H137 (= H189), D221 (= D295), V223 (= V297), Q224 (= Q298), K250 (= K324)
Q9X2A5 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
35% identity, 83% coverage: 76:473/477 of query aligns to 10:383/385 of Q9X2A5
- GT 94:95 (= GT 161:162) binding pyridoxal 5'-phosphate
- T268 (= T352) binding pyridoxal 5'-phosphate
2ordA Crystal structure of acetylornithine aminotransferase (ec 2.6.1.11) (acoat) (tm1785) from thermotoga maritima at 1.40 a resolution
35% identity, 83% coverage: 76:473/477 of query aligns to 18:391/393 of 2ordA
- active site: F134 (= F188), E186 (= E262), D219 (= D295), Q222 (= Q298), K248 (= K324), T276 (= T352), R367 (= R449)
- binding pyridoxal-5'-phosphate: G102 (= G161), T103 (= T162), F134 (= F188), H135 (= H189), E186 (= E262), D219 (= D295), V221 (= V297), Q222 (= Q298), K248 (= K324)
P73133 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
35% identity, 83% coverage: 76:472/477 of query aligns to 42:425/429 of P73133
- S125 (= S160) mutation to A: Retains 14% of N-acetylornithine aminotransferase wild-type activity.
- G126 (= G161) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- A127 (≠ T162) mutation to S: Retains 9.1% of N-acetylornithine aminotransferase wild-type activity.
- R163 (= R191) mutation to A: 4100-fold increase in KM for acetylornithine, but does not affect KM for 2-oxoglutarate. Retains 9.5% of N-acetylornithine aminotransferase wild-type activity.
- E223 (= E267) mutation to A: 65-fold increase in KM for acetylornithine, but does not affect KM for 2-oxoglutarate. Retains 50% of N-acetylornithine aminotransferase wild-type activity.; mutation to S: 73-fold increase in KM for acetylornithine, but does not affect KM for 2-oxoglutarate. Shows 160% of N-acetylornithine aminotransferase wild-type activity.
- D251 (= D295) mutation to A: Loss of N-acetylornithine aminotransferase activity.; mutation to E: Retains 20% of N-acetylornithine aminotransferase wild-type activity.
- Q254 (= Q298) mutation to A: Retains 0.9% of N-acetylornithine aminotransferase wild-type activity.
- K280 (= K324) mutation to A: Loss of N-acetylornithine aminotransferase activity.
- T308 (= T352) mutation to A: Retains 0.3% of N-acetylornithine aminotransferase wild-type activity.
- R402 (= R449) mutation to A: 2080-fold increase in KM for acetylornithine, but does not affect KM for 2-oxoglutarate. Retains 18% of N-acetylornithine aminotransferase wild-type activity.
Sites not aligning to the query:
- 39 Y→F: Retains 7.4% of N-acetylornithine aminotransferase wild-type activity.
3q8nC Crystal structure of 4-aminobutyrate transaminase from mycobacterium smegmatis (see paper)
36% identity, 87% coverage: 54:466/477 of query aligns to 14:429/439 of 3q8nC
- active site: V32 (= V72), Y151 (≠ F188), E221 (= E262), D254 (= D295), Q257 (= Q298), K283 (= K324), T312 (= T352), R412 (= R449)
- binding 4-oxobutanoic acid: G124 (= G161), A125 (≠ T162), V256 (= V297), K283 (= K324)
5lhaA Amine transaminase crystal structure from an uncultivated pseudomonas species in the pmp-bound form
33% identity, 85% coverage: 69:474/477 of query aligns to 17:445/447 of 5lhaA
- active site: Y146 (≠ F188), D253 (= D295), K282 (= K324), T319 (= T352)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G113 (= G161), S114 (≠ T162), Y146 (≠ F188), H147 (= H189), G148 (= G190), E220 (= E262), D253 (= D295), K282 (= K324), Y318 (≠ N351), T319 (= T352)
4ysnC Structure of aminoacid racemase in complex with plp (see paper)
33% identity, 83% coverage: 76:472/477 of query aligns to 34:438/448 of 4ysnC
- active site: Y149 (≠ F188), E224 (= E262), D257 (= D295), N260 (≠ Q298), K287 (= K324), T316 (= T352), R415 (= R449)
- binding pyridoxal-5'-phosphate: S121 (= S160), G122 (= G161), S123 (≠ T162), Y149 (≠ F188), H150 (= H189), E224 (= E262), D257 (= D295), V259 (= V297), K287 (= K324), F315 (≠ N351), T316 (= T352)
Sites not aligning to the query:
5lh9D Amine transaminase crystal structure from an uncultivated pseudomonas species in the plp-bound (internal aldimine) form
33% identity, 85% coverage: 69:474/477 of query aligns to 19:447/449 of 5lh9D
- active site: Y148 (≠ F188), D255 (= D295), K284 (= K324), T321 (= T352)
- binding pyridoxal-5'-phosphate: G115 (= G161), S116 (≠ T162), Y148 (≠ F188), H149 (= H189), G150 (= G190), E222 (= E262), D255 (= D295), V257 (= V297), K284 (= K324)
Query Sequence
>WP_011022811.1 NCBI__GCF_000007345.1:WP_011022811.1
MWEEGGSILDYGEPETLEKWRNSEKTEKSEDPMRKQETELDFFEQEIGLLDVVGPRAREI
IGQDCKVMSACVSRPYPLVVDRAKGSVIKDIDGKEYIDFIAGIAVMNSGHSNPEVNAAIS
AQLEKMVHCGYGDFFAEPPLKLAKKLRELSGYSKVFYCNSGTEAVEAAMKLALWKTKRPN
FIAFYNAFHGRTLGALSLTCSKVRQKEHFPTMRTVHTHYAYCYRCPLNLEYPSCGVECAK
QIENLIFRKELSPEDTAAVFIEPVQGEGGYIVPPQEFHKEVKRICTDNDVLLIADEVQTG
CFRTGPFLAMENFEVRADITCLAKALGAGLPIGAMLADSTLMDWPPGVHSNTFGGNLLSS
ASALASLEFLEKENMENRVREMGTHIRQRLRELQENCPCIGDVRGLGLMIGAEIVKSDKS
IDPIRRDRIVREAFKEGVLLLPCGDSVIRFSPPLVMTDEEADLGLDKFEKALRRAAK
Or try a new SitesBLAST search
SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory